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Sedimentation equilibrium data for wild-type SARS 3CL proteinase performed at 20 °C with three different rotor speeds (15,000, 20,000, and 25,000 rpm) and three different enzyme concentrations (0.2, 0.3, and 0.5 mg/ml). The bottom panel is the nine equilibrium data and the best fit (solid line); the upper panel is the residuals’ plot. The dissociation constant (Kd) was determined to be 14.0 μM.
